CDK8 Kinase Phosphorylates Transcription Factor STAT1 to Selectively Regulate the Interferon Response
Open accessAbstract
Gene regulation by cytokine-activated transcription factors of the signal transducer and activator of transcription (STAT) family requires serine phosphorylation within the transactivation domain (TAD). STAT1 and STAT3 TAD phosphorylation occurs upon promoter binding by an unknown kinase. Here, we show that the cyclin-dependent kinase 8 (CDK8) module of the Mediator complex phosphorylated regulatory sites within the TADs of STAT1, STAT3, and STAT5, including S727 within the STAT1 TAD in the interferon (IFN) signaling pathway. We also observed a CDK8 requirement for IFN-γ-inducible antiviral responses. Microarray analyses revealed that CDK8-mediated STAT1 phosphorylation positively or negatively regulated over 40% of IFN-γ-responsive genes, and RNA polymerase II occupancy correlated with gene expression changes. This divergent regulation occurred despite similar CDK8 occupancy at both S727 phosphorylation-dependent and -independent genes. These data identify CDK8 as a key regulator of STAT1 and antiviral responses and suggest a general role for CDK8 in STAT-mediated transcription. As such, CDK8 represents a promising target for therapeutic manipulation of cytokine responses.
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In macrophages, CDK8 is the main kinase driving STAT1 serine phosphorylation in response to IFN gamma stimulation.
“In macrophages, CDK8 appears to be the main kinase driving STAT1 serine phosphorylation in response to IFN gamma stimulation”
From CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci (2020) · cites this paper as Bancerek et al., 2013
The Results section ('CDK8 Phosphorylates S727') shows that CDK8 silencing reduced IFN-γ-induced STAT1 S727 phosphorylation more than CDK9 silencing, but those experiments were in fibroblasts. In bone-marrow-derived macrophages, the Results section ('A Nuclear CDK Mediates Canonical TAD Serine Phosphorylation') shows inhibition by flavopiridol, which is not specific to CDK8. The paper therefore supports CDK8 as a key kinase in this response, but does not establish that it is the main kinase specifically in macrophages. (LLM, conf=0.86)
Experimental — accuracy not yet measuredCDKs are regulators of STAT1 serine phosphorylation in different systems.
“Previous studies have described CDKs as regulators of STAT1 Ser phosphorylation in different systems”
From CDK8 fine-tunes IL-6 transcriptional activities by limiting STAT3 resident time at the gene loci (2020) · cites this paper as Bancerek et al., 2013
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STATs: transcriptional control and biological impact
Levy, D. E., & Darnell, J. E. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm909 · Cited by 3,201 · see citing works
Todaro, G. J., & Green, H. (1963) · The Journal of Cell Biology · doi:10.1083/jcb.17.2.299 · Cited by 2,725 · see citing works
Wen, Z., Zhong, Z., & Darnell, J. E. (1995) · Cell · doi:10.1016/0092-8674(95)90311-9 · Cited by 1,974 · see citing works
Mediator and cohesin connect gene expression and chromatin architecture
Kagey, M. H., Newman, J. J., Bilodeau, S., Zhan, Y., Orlando, D. A., van Berkum, N. L., Ebmeier, C. C., Goossens, J., Rahl, P. B., Levine, S. S., et al. (2010) · Nature · doi:10.1038/nature09380 · Cited by 1,939 · see citing works
Self-citationTargeted Disruption of the Mouse Stat1 Gene Results in Compromised Innate Immunity to Viral Disease
Durbin, J. E., Hackenmiller, R., Simon, M. C., & Levy, D. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81289-1 · Cited by 1,522 · see citing works
Serine phosphorylation of STATs
Decker, T., & Kovarik, P. (2000) · Oncogene · doi:10.1038/sj.onc.1203481 · Cited by 887 · see citing works
Self-citationNuclear CDKs Drive Smad Transcriptional Activation and Turnover in BMP and TGF-β Pathways
Alarcón, C., Zaromytidou, A.-I., Xi, Q., Gao, S., Yu, J., Fujisawa, S., Barlas, A., Miller, A. N., Manova-Todorova, K., Macias, M. J., et al. (2009) · Cell · doi:10.1016/j.cell.2009.09.035 · Cited by 719 · see citing works
Immune Control of Tuberculosis by IFN-γ-Inducible LRG-47
MacMicking, J. D., Taylor, G. A., & McKinney, J. D. (2003) · Science · doi:10.1126/science.1088063 · Cited by 685 · cited 1× · see citing works
“Primary Irf1, Wars (also known as Ifp-53), and Ifi47 are each regulated by binding of the STAT1 homodimer to the IFN-g-activated sequence (GAS) in the promoter (MacMicking et al., 2003; Pine et al., 1994; Strehlow et al., 1993).”
CDK8 is a colorectal cancer oncogene that regulates β-catenin activity
Firestein, R., Bass, A. J., Kim, S. Y., Dunn, I. F., Silver, S. J., Guney, I., Freed, E., Ligon, A. H., Vena, N., Ogino, S., et al. (2008) · Nature · doi:10.1038/nature07179 · Cited by 678 · see citing works
Mastermind Recruits CycC:CDK8 to Phosphorylate the Notch ICD and Coordinate Activation with Turnover
Fryer, C. J., White, B., & Jones, K. A. (2004) · Molecular Cell · doi:10.1016/j.molcel.2004.10.014 · Cited by 627 · see citing works
Flavopiridol Inactivates P-TEFb and Blocks Most RNA Polymerase II Transcription in Vivo
Chao, S., & Price, D. H. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m102306200 · Cited by 623 · see citing works
Cracking the RNA polymerase II CTD code
Egloff, S., & Murphy, S. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.03.008 · Cited by 408 · see citing works
Dölken, L., Ruzsics, Z., Rädle, B., Friedel, C. C., Zimmer, R., Mages, J., Hoffmann, R. F. G., Dickinson, P., Forster, T., Ghazal, P., et al. (2008) · RNA · doi:10.1261/rna.1136108 · Cited by 407 · see citing works
Self-citationTFIIH is negatively regulated by cdk8-containing mediator complexes
Akoulitchev, S., Chuikov, S., & Reinberg, D. (2000) · Nature · doi:10.1038/35024111 · Cited by 393 · see citing works
CDK8 is a positive regulator of transcriptional elongation within the serum response network
Donner, A. J., Ebmeier, C. C., Taatjes, D. J., & Espinosa, J. M. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1752 · Cited by 368 · see citing works
Self-citationWada, T., Takagi, T., Yamaguchi, Y., Watanabe, D., & Handa, H. (1998) · The EMBO Journal · doi:10.1093/emboj/17.24.7395 · Cited by 355 · see citing works
The human CDK8 subcomplex is a molecular switch that controls Mediator coactivator functionPreprint
Knuesel, M. T., Meyer, K. D., Bernecky, C., & Taatjes, D. J. (2009) · Genes & Development · doi:10.1101/gad.1767009 · Cited by 350 · see citing works
Self-citationPine, R., Canova, A., & Schindler, C. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06245.x · Cited by 347 · see citing works
Human Mediator Subunit MED26 Functions as a Docking Site for Transcription Elongation Factors
Takahashi, H., Parmely, T. J., Sato, S., Tomomori‐Sato, C., Banks, C. A. S., Kong, S. E., Szutorisz, H., Swanson, S. K., Martin‐Brown, S., Washburn, M. P., et al. (2011) · Cell · doi:10.1016/j.cell.2011.06.005 · Cited by 346 · see citing works
Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes
Yang, J., Huang, J., Dasgupta, M., Sears, N., Miyagi, M., Wang, B., Chance, M. R., Chen, X., Du, Y., Wang, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016147107 · Cited by 340 · see citing works
The human Mediator complex: a versatile, genome-wide regulator of transcription
Taatjes, D. J. (2010) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.02.004 · Cited by 327 · see citing works
Self-citationE2F1 represses β-catenin transcription and is antagonized by both pRB and CDK8
Morris, E. J., Ji, J., Yang, F., Stefano, L. D., Herr, A., Moon, N. S., Kwon, E. J., Haigis, K. M., Näär, A. M., & Dyson, N. J. (2008) · Nature · doi:10.1038/nature07310 · Cited by 297 · see citing works
Canonical and non-canonical JAK–STAT signaling
Li, W. X. (2008) · Trends in Cell Biology · doi:10.1016/j.tcb.2008.08.008 · Cited by 290 · see citing works
Varinou, L., Ramsauer, K., Karaghiosoff, M., Kolbe, T., Pfeffer, K., Müller, M., & Decker, T. (2003) · Immunity · doi:10.1016/s1074-7613(03)00322-4 · Cited by 284 · see citing works
Self-citationLew, D. J., Decker, T., Strehlow, I., & Darnell, J. E., Jr. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.1.182 · Cited by 280 · see citing works
Kovarik, P., Stoiber, D., Eyers, P. A., Menghini, R., Neininger, A., Gaestel, M., Cohen, P., & Decker, T. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13956 · Cited by 271 · see citing works
Self-citationStat1 combines signals derived from IFN‐γ and LPS receptors during macrophage activation
Kovarik, P., Stoiber, D., Novy, M., & Decker, T. (1998) · The EMBO Journal · doi:10.1093/emboj/17.13.3660 · Cited by 243 · see citing works
Self-citationThe cyclin-dependent kinase 8 module sterically blocks Mediator interactions with RNA polymerase II
Elmlund, H., Baraznenok, V., Lindahl, M., Samuelsen, C. O., Koeck, P. J. B., Holmberg, S., Hebert, H., & Gustafsson, C. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607483103 · Cited by 230 · see citing works
Knuesel, M. T., Meyer, K. D., Donner, A. J., Espinosa, J. M., & Taatjes, D. J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.00993-08 · Cited by 226 · see citing works
Self-citationIFN-inducible GTPases and immunity to intracellular pathogens
MacMicking, J. D. (2004) · Trends in Immunology · doi:10.1016/j.it.2004.08.010 · Cited by 221 · see citing works
Regulation of lipogenesis by cyclin-dependent kinase 8–mediated control of SREBP-1
Zhao, X., Feng, D., Wang, Q., Abdulla, A., Xie, X.-J., Zhou, J., Sun, Y., Yang, E. S. T., Liu, L., Vaitheesvaran, B., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci61462 · Cited by 214 · see citing works
Mediator Requirement for Both Recruitment and Postrecruitment Steps in Transcription Initiation
Wang, G., Balamotis, M. A., Stevens, J. L., Yamaguchi, Y., Handa, H., & Berk, A. J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.02.010 · Cited by 211 · see citing works
Morinobu, A., Gadina, M., Strober, W., Visconti, R., Fornace, A. J., Montagna, C., Feldman, G. M., Nishikomori, R., & O’Shea, J. J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.182618999 · Cited by 207 · see citing works
Shen, Y., Schlessinger, K., Zhu, X., Meffre, E., Quimby, F., Levy, D. E., & Darnell, J. E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.407-419.2004 · Cited by 200 · see citing works
Kovarik, P., Mangold, M., Ramsauer, K., Heidari, H., Steinborn, R., Zotter, A., Levy, D. E., Müller, M., & Decker, T. (2001) · The EMBO Journal · doi:10.1093/emboj/20.1.91 · Cited by 198 · see citing works
Self-citationRegulation of CDK7 substrate specificity by MAT1 and TFIIH
Yankulov, K., & Bentley, D. L. (1997) · The EMBO Journal · doi:10.1093/emboj/16.7.1638 · Cited by 181 · see citing works
Sadzak, I., Schiff, M., Gattermeier, I., Glinitzer, R., Sauer, I., Saalmüller, A., Yang, E., Schaljo, B., & Kovarik, P. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0801794105 · Cited by 166 · see citing works
Self-citationp53 activates transcription by directing structural shifts in Mediator
Meyer, K. D., Lin, S., Bernecky, C., Gao, Y., & Taatjes, D. J. (2010) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1816 · Cited by 144 · see citing works
Self-citationCdk8 Is Essential for Preimplantation Mouse Development
Westerling, T., Kuuluvainen, E., & Mäkelä, T. P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01302-06 · Cited by 141 · see citing works
Alessi, F., Quarta, S., Savio, M., Riva, F., Rossi, L. H., Stivala, L. A., Scovassi, A. I., Meijer, L., & Prosperi, E. (1998) · Experimental Cell Research · doi:10.1006/excr.1998.4216 · Cited by 139 · see citing works
Cyclin C/CDK8 and cyclin H/CDK7/p36 are biochemically distinct CTD kinases
Rickert, P., Corden, J. L., & Lees, E. M. (1999) · Oncogene · doi:10.1038/sj.onc.1202399 · Cited by 122 · see citing works
Activator-Mediator binding regulates Mediator-cofactor interactions
Ebmeier, C. C., & Taatjes, D. J. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0914215107 · Cited by 116 · see citing works
Self-citationMeyer, K. D., Donner, A. J., Knuesel, M. T., York, A. G., Espinosa, J. M., & Taatjes, D. J. (2008) · The EMBO Journal · doi:10.1038/emboj.2008.78 · Cited by 105 · see citing works
Self-citationDistinct roles for Mediator Cdk8 module subunits in Drosophila development
Loncle, N., Boube, M., Joulia, L., Boschiero, C., Werner, M., Cribbs, D. L., & Bourbon, H.-M. G. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601566 · Cited by 100 · see citing works
Complexity in Transcription Control at the Activation Domain–Mediator Interface
Balamotis, M. A., Pennella, M. A., Stevens, J. L., Wasylyk, B., Belmont, A. S., & Berk, A. J. (2009) · Science Signaling · doi:10.1126/scisignal.1164302 · Cited by 84 · see citing works
Strehlow, I., Seegert, D., Frick, C., Bange, F. C., Schindler, C., Böttger, E. C., & Decker, T. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85460-1 · Cited by 66 · see citing works
Regulation of IFN Consensus Sequence Binding Protein Expression in Murine Macrophages
Kantakamalakul, W., Politis, A. D., Marecki, S., Sullivan, T., Ozato, K., Fenton, M. J., & Vogel, S. N. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.162.12.7417 · Cited by 61 · see citing works
Stat5a serine 725 and 779 phosphorylation is a prerequisite for hematopoietic transformation
Friedbichler, K., Kerenyi, M. A., Kovačic, B., Li, G., Hoelbl‐Kovacic, A., Yahiaoui, S., Sexl, V., Müllner, E. W., Fajmann, S., Cerny‐Reiterer, S., et al. (2010) · Blood · doi:10.1182/blood-2009-12-258913 · Cited by 60 · see citing works
Nguyen, T. T., Hu, Y., Widney, D. P., Mar, R., & Smith, J. B. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002760274926 · Cited by 56 · see citing works
Kubosaki, A., Lindgren, G., Tagami, M., Simon, C., Tomaru, Y., Miura, H., Suzuki, T., Arner, E., Forrest, A. R. R., Irvine, K. M., et al. (2010) · Molecular Immunology · doi:10.1016/j.molimm.2010.05.289 · Cited by 29 · see citing works
Review: IRF-4 Activities in HTLV-I-Induced T Cell Leukemogenesis
Mamane, Y., Sharma, S., Grandvaux, N., Hernandez, E., & Hiscott, J. B. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753452746 · Cited by 28 · see citing works
Flagged first, then by citations
2 of the 53 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Regulation of type I interferon responses
Ivashkiv, L. B., & Donlin, L. T. (2013) · Nature reviews. Immunology · doi:10.1038/nri3581 · Cited by 3,311 · see citing works
IFNγ: signalling, epigenetics and roles in immunity, metabolism, disease and cancer immunotherapy
Ivashkiv, L. B. (2018) · Nature reviews. Immunology · doi:10.1038/s41577-018-0029-z · Cited by 1,374 · see citing works
Mechanisms and consequences of Jak–STAT signaling in the immune system
Villarino, A. V., Kanno, Y., & O'Shea, J. J. (2017) · Nature Immunology · doi:10.1038/ni.3691 · Cited by 1,221 · see citing works
The Mediator complex: a central integrator of transcription
Allen, B. L., & Taatjes, D. J. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3951 · Cited by 922 · see citing works
Self-citationMechanisms of Jak/STAT Signaling in Immunity and Disease
Villarino, A. V., Kanno, Y., Ferdinand, J. R., & O’Shea, J. J. (2014) · The Journal of Immunology · doi:10.4049/jimmunol.1401867 · Cited by 554 · see citing works
Mediator kinase inhibition further activates super-enhancer-associated genes in AML
Pelish, H. E., Liau, B. B., Nitulescu, I. I., Tangpeerachaikul, A., Poss, Z. C., Silva, D. H. D., Caruso, B., Arefolov, A., Fadeyi, O., Christie, A. L., et al. (2015) · Nature · doi:10.1038/nature14904 · Cited by 397 · see citing works
Self-citationGenome-Scale Identification of SARS-CoV-2 and Pan-coronavirus Host Factor Networks
Schneider, W. M., Luna, J. M., Hoffmann, H.-H., Rivera, F. J. S., Leal, A. A., Ashbrook, A. W., Pen, J. L., Ricardo-Lax, I., Michailidis, E., Peace, A., et al. (2020) · Cell · doi:10.1016/j.cell.2020.12.006 · Cited by 404 · see citing works
Inhibitors of cyclin-dependent kinases as cancer therapeutics.
Whittaker, S. R., Mallinger, A., Workman, P., & Clarke, P. A. (2017) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2017.02.008 · Cited by 384 · see citing works
The Mediator complex and transcription regulation
Poss, Z. C., Ebmeier, C. C., & Taatjes, D. J. (2013) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2013.840259 · Cited by 364 · see citing works
Self-citationMajoros, A., Platanitis, E., Kernbauer, E., Rosebrock, F., Müller, M. M., & Decker, T. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00029 · Cited by 321 · see citing works
Self-citationCyclin-dependent protein kinases and cell cycle regulation in biology and disease
Pellarin, I., Dall'Acqua, A., Favero, A., Segatto, I., Rossi, V., Crestan, N., Karimbayli, J., Belletti, B., & Baldassarre, G. (2025) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-024-02080-z · Cited by 323 · see citing works
BET inhibition blocks inflammation-induced cardiac dysfunction and SARS-CoV-2 infection
Mills, R. J., Humphrey, S. J., Fortuna, P. R. J., Lor, M., Foster, S. R., Quaife-Ryan, G. A., Johnston, R. L., Dumenil, T. D., Bishop, C., Rudraraju, R., et al. (2021) · Cell · doi:10.1016/j.cell.2021.03.026 · Cited by 223 · see citing works
Transcriptional Regulation of Antiviral Interferon-Stimulated Genes
Wang, W., Xu, L., Su, J., Peppelenbosch, M. P., & Pan, Q. (2017) · Trends in Microbiology · doi:10.1016/j.tim.2017.01.001 · Cited by 221 · see citing works
Differential Regulation of Type I and Type III Interferon Signaling
Stanifer, M. L., Pervolaraki, K., & Boulant, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061445 · Cited by 214 · see citing works
The Mediator Complex: At the Nexus of RNA Polymerase II Transcription
Jerónimo, C., & Robert, F. (2017) · Trends in Cell Biology · doi:10.1016/j.tcb.2017.07.001 · Cited by 189 · see citing works
Immunomodulation by anticancer cell cycle inhibitors
Petroni, G., Formenti, S. C., Chen-Kiang, S., & Galluzzi, L. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-020-0300-y · Cited by 163 · see citing works
Targeting transcription cycles in cancer
Vervoort, S., Devlin, J., Kwiatkowski, N., Teng, M.-X., Gray, N., & Johnstone, R. (2021) · Nature Reviews. Cancer · doi:10.1038/s41568-021-00411-8 · Cited by 140 · see citing works
Poss, Z. C., Ebmeier, C. C., Odell, A. T., Tangpeerachaikul, A., Lee, T., Pelish, H. E., Shair, M. D., Dowell, R. D., Old, W. M., & Taatjes, D. J. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.03.030 · Cited by 160 · see citing works
Self-citationNPR1 Promotes Its Own and Target Gene Expression in Plant Defense by Recruiting CDK8
Chen, J., Mohan, R., Zhang, Y., Li, M., Chen, H., Palmer, I. A., Chang, M., Qi, G., Spoel, S. H., Mengiste, T. D., et al. (2019) · PLANT PHYSIOLOGY · doi:10.1104/pp.19.00124 · Cited by 150 · see citing works
Akamatsu, M., Mikami, N., Ohkura, N., Kawakami, R., Kitagawa, Y., Sugimoto, A., Hirota, K., Nakamura, N., Ujihara, S., Kurosaki, T., et al. (2019) · Science Immunology · doi:10.1126/sciimmunol.aaw2707 · Cited by 148 · see citing works
A selective chemical probe for exploring the role of CDK8 and CDK19 in human disease
Dale, T. C., Clarke, P. A., Esdar, C., Waalboer, D., Adeniji-Popoola, O., Ortiz-Ruiz, M.-J., Mallinger, A., Samant, R. S., Czodrowski, P., Müsil, D., et al. (2015) · Nature Chemical Biology · doi:10.1038/nchembio.1952 · Cited by 146 · see citing works
Nan, Y., Wu, C., & Zhang, Y. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.01758 · Cited by 142 · see citing works
CDK8/19 Mediator kinases potentiate induction of transcription by NFκB
Chen, M., Liang, J., Ji, H., Yang, Z., Altilia, S., Hu, B., Schronce, A., McDermott, M. S. J., Schools, G. P., Lim, C., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710467114 · Cited by 141 · see citing works
Kang, K., Bachu, M., Park, S. H., Kang, K., Bae, S., Park‐Min, K., & Ivashkiv, L. B. (2019) · Nature Communications · doi:10.1038/s41467-019-11147-3 · Cited by 139 · see citing works
Set1/COMPASS and Mediator are repurposed to promote epigenetic transcriptional memory
D’Urso, A., Takahashi, Y.-H., Xiong, B., Marone, J., Coukos, R., Randise-Hinchliff, C., Wang, J.-P., Shilatifard, A., & Brickner, J. H. (2016) · eLife · doi:10.7554/elife.16691 · Cited by 133 · see citing works
CDK8-Mediated STAT1-S727 Phosphorylation Restrains NK Cell Cytotoxicity and Tumor Surveillance
Putz, E. M., Gotthardt, D., Hoermann, G., Csiszar, A., Wirth, S., Berger, A., Straka, E., Rigler, D., Wallner, B., Jamieson, A. M., et al. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.07.012 · Cited by 132 · see citing works
Self-citationRegulatory functions of the Mediator kinases CDK8 and CDK19
Fant, C. B., & Taatjes, D. J. (2018) · Transcription · doi:10.1080/21541264.2018.1556915 · Cited by 122 · see citing works
Self-citationCzodrowski, P., Mallinger, A., Wienke, D., Esdar, C., Pöschke, O., Busch, M., Rohdich, F., Eccles, S. A., Ortiz-Ruiz, M.-J., Schneider, R., et al. (2016) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.6b00597 · Cited by 123 · see citing works
Mediator kinase module and human tumorigenesis
Clark, A. D., Oldenbroek, M., & Boyer, T. (2015) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.3109/10409238.2015.1064854 · Cited by 115 · see citing works
Rzymski, T., Mikuła, M., Żyłkiewicz, E., Dreas, A., Wiklik, K., Gołas, A., Wójcik, K., Masiejczyk, M., Wróbel, A., Dolata, I., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.16810 · Cited by 117 · see citing works
The two faces of Cdk8, a positive/negative regulator of transcription
Nemet, J., Jelicic, B., Rubelj, I., & Sopta, M. (2014) · Biochimie · doi:10.1016/j.biochi.2013.10.004 · Cited by 115 · see citing works
Cyclin-Dependent Kinase 8: A New Hope in Targeted Cancer Therapy?
Philip, S., Kumarasiri, M., Teo, T., Yu, M., & Wang, S. (2017) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.7b00901 · Cited by 111 · see citing works
The Mediator kinase module: an interface between cell signaling and transcription
Luyties, O., & Taatjes, D. J. (2022) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2022.01.002 · Cited by 102 · see citing works
Self-citationSteinparzer, I., Sedlyarov, V., Rubin, J. D., Eislmayr, K., Galbraith, M. D., Levandowski, C. B., Vcelkova, T., Sneezum, L., Wascher, F., Amman, F., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.07.034 · Cited by 105 · see citing works
Self-citationDissecting the Pol II transcription cycle and derailing cancer with CDK inhibitors
Parua, P. K., & Fisher, R. P. (2020) · Nature Chemical Biology · doi:10.1038/s41589-020-0563-4 · Cited by 104 · see citing works
Clarke, P. A., Ortiz-Ruiz, M.-J., Poele, R. T., Adeniji-Popoola, O., Box, G., Court, W., Czasch, S., Bawab, S. E., Esdar, C., Ewan, K., et al. (2016) · eLife · doi:10.7554/elife.20722 · Cited by 99 · see citing works
CDK8 Kinase Activity Promotes Glycolysis
Galbraith, M. D., Andrysík, Z., Pandey, A., Hoh, M., Bonner, E. A., Hill, A. A., Sullivan, K. D., & Espinosa, J. M. (2017) · Cell Reports · doi:10.1016/j.celrep.2017.10.058 · Cited by 96 · see citing works
Development of Highly Potent and Selective Steroidal Inhibitors and Degraders of CDK8
Hatcher, J. M., Wang, E. S., Johannessen, L. H., Kwiatkowski, N. P., Sim, T., & Gray, N. S. (2018) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.8b00011 · Cited by 94 · see citing works
Liang, J., Chen, M., Hughes, D. T., Chumanevich, A. A., Altilia, S., Kaza, V., Lim, C., Kiaris, H., Mythreye, K., Peña, M. M. O., et al. (2018) · Cancer Research · doi:10.1158/0008-5472.can-18-1583 · Cited by 91 · see citing works
Molecular and in vivo Functions of the CDK8 and CDK19 Kinase Modules
Dannappel, M., Sooraj, D., Loh, J. J., & Firestein, R. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2018.00171 · Cited by 88 · see citing works
Fish, E. N., & Platanias, L. C. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0450 · Cited by 87 · see citing works
Development of a Potent, Specific CDK8 Kinase Inhibitor Which Phenocopies CDK8/19 Knockout Cells
Koehler, M. F. T., Bergeron, P., Blackwood, E. M., Bowman, K. K., Clark, K., Firestein, R., Kiefer, J. R., Maskos, K., McCleland, M. L., Orren, L., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.5b00278 · Cited by 81 · see citing works
Tymoszuk, P., Charoentong, P., Hackl, H., Seeboeck, R., Müller‐Holzner, E., Trajanoski, Z., Obrist, P., Révillion-Carette, F., Peyrat, J., Fiegl, H., et al. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-257 · Cited by 79 · see citing works
A Kinase-Independent Role for Cyclin-Dependent Kinase 19 in p53 Response
Audetat, K. A., Galbraith, M. D., Odell, A. T., Lee, T., Pandey, A., Espinosa, J. M., Dowell, R. D., & Taatjes, D. J. (2017) · Molecular and Cellular Biology · doi:10.1128/mcb.00626-16 · Cited by 75 · see citing works
Self-citationCDK8 kinase—An emerging target in targeted cancer therapy
Rzymski, T., Mikuła, M., Wiklik, K., & Brzózka, K. D. (2015) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2015.05.011 · Cited by 76 · see citing works
STAT5A and STAT5B—Twins with Different Personalities in Hematopoiesis and Leukemia
Maurer, B., Kollmann, S., Pickem, J., Hoelbl‐Kovacic, A., & Sexl, V. (2019) · Cancers · doi:10.3390/cancers11111726 · Cited by 77 · see citing works
New roles for cyclin-dependent kinases in T cell biology: linking cell division and differentiation
Wells, A. D., & Morawski, P. A. (2014) · Nature reviews. Immunology · doi:10.1038/nri3625 · Cited by 77 · see citing works
Selective and Potent CDK8/19 Inhibitors Enhance NK-Cell Activity and Promote Tumor Surveillance
Hofmann, M. H., Mani, R., Engelhardt, H., Impagnatiello, M. A., Carotta, S., Kerenyi, M. A., Lorenzo‐Herrero, S., Böttcher, J., Scharn, D., Arnhof, H., et al. (2020) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-19-0789 · Cited by 76 · see citing works
A precisely positioned MED12 activation helix stimulates CDK8 kinase activity
Klatt, F., Leitner, A., Kim, I. V., Ho-Xuan, H., Schneider, E. V., Langhammer, F., Weinmann, R., Müller, M., Huber, R., Meister, G., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1917635117 · Cited by 75 · see citing works
Self-citationNuclear RNF2 inhibits interferon function by promoting K33-linked STAT1 disassociation from DNA
Liu, S., Jiang, M., Wang, W., Liu, W., Song, X., Ma, Z., Zhang, S., Liu, L., Liu, Y., & Cao, X. (2017) · Nature Immunology · doi:10.1038/s41590-017-0003-0 · Cited by 76 · see citing works
Saleiro, D., & Platanias, L. C. (2019) · Seminars in Immunology · doi:10.1016/j.smim.2019.101299 · Cited by 72 · see citing works
Chen, M., Li, J., Zhang, L., Wang, L., Cheng, C., Ji, H., Altilia, S., Ding, X., Cai, G., Altomare, D., et al. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad538 · Cited by 73 · see citing works
Small-molecule studies identify CDK8 as a regulator of IL-10 in myeloid cells
Johannessen, L. H., Sundberg, T. B., O'Connell, D. J., Kolde, R., Berstler, J., Billings, K., Khor, B., Seashore-Ludlow, B. A., Fassl, A., Russell, C. N., et al. (2017) · Nature Chemical Biology · doi:10.1038/nchembio.2458 · Cited by 73 · see citing works
Cyclin-dependent kinase activity is required for type I interferon production
Cingöz, O., & Goff, S. P. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1720431115 · Cited by 68 · see citing works
A kinase-independent role for CDK8 in BCR-ABL1+ leukemia
Menzl, I., Zhang, T., Berger‐Becvar, A., Grausenburger, R., Heller, G., Prchal‐Murphy, M., Edlinger, L., Knab, V. M., Uras, I. Z., Grundschober, E., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12656-x · Cited by 68 · see citing works
CDK8 maintains stemness and tumorigenicity of glioma stem cells by regulating the c-MYC pathway
Fukasawa, K., Kadota, T., Horie, T., Tokumura, K., Terada, R., Kitaguchi, Y., Park, G., Ochiai, S., Iwahashi, S., Okayama, Y., et al. (2021) · Oncogene · doi:10.1038/s41388-021-01745-1 · Cited by 68 · see citing works
Calpena, E., Hervieu, A., Kaserer, T., Swagemakers, S. M. A., Goos, J. A. C., Adeniji-Popoola, O., Ortiz-Ruiz, M. J., Barbaro‐Dieber, T., Bownass, L., Brilstra, E. H., et al. (2019) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2019.02.006 · Cited by 66 · see citing works
Wienerroither, S., Shukla, P., Farlik, M., Majoros, A., Stych, B., Vogl, C., Cheon, H., Stark, G. R., Strobl, B., Müller, M. M., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.06.021 · Cited by 63 · see citing works
Self-citationLynch, C. J., Bernad, R., Martínez‐Val, A., Shahbazi, M. N., Pereira, S. N., Calvo, I., Blanco‐Aparicio, C., Tarantino, C., Garreta, E., Richart, L., et al. (2020) · Nature Cell Biology · doi:10.1038/s41556-020-0573-1 · Cited by 61 · see citing works
Design and Development of a Series of Potent and Selective Type II Inhibitors of CDK8
Bergeron, P., Koehler, M. F. T., Blackwood, E. M., Bowman, K. K., Clark, K., Firestein, R., Kiefer, J. R., Maskos, K., McCleland, M. L., Orren, L., et al. (2016) · ACS Medicinal Chemistry Letters · doi:10.1021/acsmedchemlett.6b00044 · Cited by 62 · see citing works
Tian, B., Zhao, Y., Kalita, M. K., Edeh, C. B., Paessler, S., Casola, A., Teng, M. N., Garofalo, R. P., & Brasier, A. R. (2013) · Journal of Virology · doi:10.1128/jvi.03399-12 · Cited by 61 · see citing works
PAK-dependent STAT5 serine phosphorylation is required for BCR-ABL-induced leukemogenesis
Berger, A., Hoelbl‐Kovacic, A., Bourgeais, J., Hoefling, L., Warsch, W., Grundschober, E., Uras, I. Z., Menzl, I., Putz, E. M., Hoermann, G., et al. (2013) · Leukemia · doi:10.1038/leu.2013.351 · Cited by 60 · see citing works
Chen, M., Li, J., Liang, J., Thompson, Z. S., Kathrein, K., Broude, E. V., & Roninson, I. B. (2019) · Cells · doi:10.3390/cells8111413 · Cited by 57 · see citing works
Genetic landscape of T- and NK-cell post-transplant lymphoproliferative disorders
Margolskee, E. M., Jobanputra, V., Jain, P., Chen, J., Ganapathi, K. A., Nahum, O., Levy, B., Morscio, J., Murty, V., Tousseyn, T., et al. (2016) · OncoTarget · doi:10.18632/oncotarget.9400 · Cited by 55 · see citing works
Walker, E. C., Johnson, R. W., Hu, Y., Brennan, H. J., Poulton, I. J., Zhang, J., Jenkins, B. J., Smyth, G. K., Nicola, N. A., & Sims, N. A. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.748483 · Cited by 57 · see citing works
Majoros, A., Platanitis, E., Szappanos, D., Cheon, H., Vogl, C., Shukla, P., Stark, G. R., Sexl, V., Schreiber, R. D., Schindler, C., et al. (2016) · EMBO Reports · doi:10.15252/embr.201540726 · Cited by 55 · see citing works
Self-citationLloyd, R. L., Urban, V., Muñoz‐Martínez, F., Ayestaran, I., Thomas, J. C., de Renty, C., O’Connor, M. J., Forment, J. V., Galanty, Y., & Jackson, S. P. (2021) · Nucleic Acids Research · doi:10.1093/nar/gkab628 · Cited by 54 · see citing works
Guo, Z., Wang, G., Lv, Y., Wan, Y. Y., & Zheng, J. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.01988 · Cited by 54 · see citing works
Angel or Devil ? - CDK8 as the new drug target
Wu, D., Zhang, Z., Chen, X., Yan, Y., & Liu, X. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.113043 · Cited by 53 · see citing works
Mediator Kinase Phosphorylation of STAT1 S727 Promotes Growth of Neoplasms With JAK-STAT Activation
Niţulescu, I., Meyer, S. C., Wen, Q. J., Crispino, J. D., Lemieux, M. E., Levine, R. L., Pelish, H. E., & Shair, M. D. (2017) · EBioMedicine · doi:10.1016/j.ebiom.2017.11.013 · Cited by 53 · see citing works
CDK8-Novel Therapeutic Opportunities
Menzl, I., Witalisz‐Siepracka, A., & Sexl, V. (2019) · Pharmaceuticals · doi:10.3390/ph12020092 · Cited by 52 · see citing works
IFNγ-induced PD-L1 expression in ovarian cancer cells is regulated by JAK1, STAT1 and IRF1 signaling
Padmanabhan, S., Gaire, B., Zou, Y., Uddin, M. M., & Vancurova, I. (2022) · Cellular Signalling · doi:10.1016/j.cellsig.2022.110400 · Cited by 52 · see citing works
Ding, X., Sharko, A. C., McDermott, M. S. J., Schools, G. P., Chumanevich, A. A., Ji, H., Li, J., Zhang, L., Mack, Z. T., Sikirzhytski, V., et al. (2022) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2201073119 · Cited by 49 · see citing works
Nakamura, A., Nakata, D., Kakoi, Y., Kunitomo, M., Murai, S., Ebara, S., Hata, A., & Hara, T. (2018) · Oncotarget · doi:10.18632/oncotarget.24414 · Cited by 48 · see citing works
STAT1 is required to establish but not maintain interferon‐γ‐induced transcriptional memory
Tehrani, S., Mikulski, P., Abdul‐Zani, I., Mata, J. F., Siwek, W., & Jansen, L. E. T. (2023) · The EMBO Journal · doi:10.15252/embj.2022112259 · Cited by 47 · see citing works
Inhibition of STAT5: A therapeutic option in BCR-ABL1-driven leukemia
Berger, A., Sexl, V., Valent, P., & Moriggl, R. (2014) · Oncotarget · doi:10.18632/oncotarget.2465 · Cited by 47 · see citing works
NK Cell–Specific CDK8 Deletion Enhances Antitumor Responses
Witalisz-Siepracka, A., Gotthardt, D., Prchal-Murphy, M., Didara, Z., Menzl, I., Prinz, D., Edlinger, L., Putz, E. M., & Sexl, V. (2018) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-17-0183 · Cited by 47 · see citing works
Increased mediator complex subunit CDK19 expression associates with aggressive prostate cancer
Becker, F., Joerg, V., Hupe, M. C., Roth, D., Krupar, R., Lubczyk, V., Kuefer, R., Sailer, V. W., Duensing, S. M., Kirfel, J., et al. (2019) · International Journal of Cancer · doi:10.1002/ijc.32551 · Cited by 47 · see citing works
CDK8 Fine-Tunes IL-6 Transcriptional Activities by Limiting STAT3 Resident Time at the Gene Loci
Martínez‐Fábregas, J., Wang, L., Pöhler, E., Cozzani, A., Wilmes, S., Kazemian, M., Mitra, S., & Moraga, I. (2020) · Cell Reports · doi:10.1016/j.celrep.2020.108545 · Cited by 47 · see citing works
Nuclear ADP-ribosylation drives IFNγ-dependent STAT1α enhancer formation in macrophages
Gupte, R., Nandu, T. S., & Kraus, W. L. (2021) · Nature Communications · doi:10.1038/s41467-021-24225-2 · Cited by 47 · see citing works
Li, X., Wang, F., Xu, X., Zhang, J., & Xu, G. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.636595 · Cited by 46 · see citing works
MED12 and BRD4 cooperate to sustain cancer growth upon loss of mediator kinase
Sooraj, D., Sun, C. X., Doan, A., Garama, D. J., Dannappel, M., Zhu, D., Chua, H. K., Mahara, S., Hassan, W. A. W., Tay, Y. K., et al. (2021) · Molecular Cell · doi:10.1016/j.molcel.2021.11.015 · Cited by 45 · see citing works
Shape-based virtual screen for the discovery of novel CDK8 inhibitor chemotypes
He, L., Zhu, Y., Fan, Q.-Z., Miao, D., Zhang, S., Liu, X., & Zhang, C. (2019) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.12.065 · Cited by 45 · see citing works
Greber, B. J., & Nogales, E. (2019) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-030-28151-9_5 · Cited by 43 · see citing works
Wang, M., Lin, R., Li, J., Suo, Y., Gao, J., Liu, L., Zhou, L., Ni, Y., Yang, Z., Zheng, J., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c02045 · Cited by 42 · see citing works
Wu, L., Qin, Y., Xia, S., Dai, M., Han, X., Wu, Y., Zhang, X., Ma, J., Wang, Y., Tang, Y., et al. (2015) · Arthritis & Rheumatology · doi:10.1002/art.39543 · Cited by 40 · see citing works
Semper, C., Leitner, N. R., Lassnig, C., Parrini, M., Mahlakõiv, T., Rammerstorfer, M., Lorenz, K., Rigler, D., Müller, S., Kolbe, T., et al. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00295-14 · Cited by 42 · see citing works
Self-citationMED 12 mutations and NOTCH signalling in chronic lymphocytic leukaemia
Wu, B., Slabicki, M. M., Sellner, L., Dietrich, S., Liu, X., Jethwa, A., Hüllein, J., Walther, T., Wagner, L., Huang, Z., et al. (2017) · British Journal of Haematology · doi:10.1111/bjh.14869 · Cited by 41 · see citing works
Zhang, L., Cheng, C., Li, J., Wang, L., Chumanevich, A. A., Porter, D. C., Mindich, A., Gorbunova, S., Roninson, I. B., Chen, M., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c01951 · Cited by 40 · see citing works
Kiritsy, M. C., Ankley, L. M., Trombley, J. D., Huizinga, G. P., Lord, A. E., Orning, P., Elling, R., Fitzgerald, K. A., & Olive, A. J. (2021) · eLife · doi:10.7554/elife.65110 · Cited by 39 · see citing works
Kościuczuk, E. M., Mehrotra, S., Saleiro, D., Kroczyńska, B., Majchrzak-Kita, B., Lisowski, P., Driehaus, C., Rogalska, A., Turner, A. E., Lienhoop, T., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.005956 · Cited by 39 · see citing works
Yamamoto, S., Hagihara, T., Horiuchi, Y., Okui, A., Wani, S., Yoshida, T., Inoué, T., Tanaka, A., Ito, T., Hirose, Y., et al. (2017) · Genes to Cells · doi:10.1111/gtc.12475 · Cited by 38 · see citing works
Miao, Y., Gambini, A., Zhang, Y., Padilla‐Banks, E., Jefferson, W. N., Bernhardt, M. L., Huang, W., Li, L., & Williams, C. J. (2018) · Biology of Reproduction · doi:10.1093/biolre/ioy004 · Cited by 37 · see citing works
Sharko, A. C., Lim, C., McDermott, M. S. J., Hennes, C., Philavong, K. P., Aiken, T., Tatarskiy, V. V., Roninson, I. B., & Broude, E. V. (2021) · Cells · doi:10.3390/cells10010144 · Cited by 37 · see citing works
Chen, T., Tsai, M.-H., Kung, J. T., Lin, K., Decker, T., & Lee, C. (2016) · The Journal of Experimental Medicine · doi:10.1084/jem.20151620 · Cited by 36 · see citing works
Ono, K., Banno, H., Okaniwa, M., Hirayama, T., Iwamura, N., Hikichi, Y., Murai, S., Hasegawa, M., Hasegawa, Y., Yonemori, K., et al. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.02.038 · Cited by 36 · see citing works
Competitive binding of STATs to receptor phospho-Tyr motifs accounts for altered cytokine responses
Wilmes, S., Jeffrey, P.-A., Martínez‐Fábregas, J., Hafer, M., Fyfe, P. K., Pöhler, E., Gaggero, S., López‐García, M., Lythe, G., Taylor, C., et al. (2021) · eLife · doi:10.7554/elife.66014 · Cited by 35 · see citing works
Transcriptional cyclin-dependent kinases: Potential drug targets in cancer therapy
Liu, Y., Fu, L., Wu, J., Liu, M., Wang, G., Liu, B., & Zhang, L. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.114056 · Cited by 35 · see citing works
Xiao, J., Liang, J., Fan, J., Hou, P., Li, X., Zhang, H., Li, K., Bu, L., Li, P., He, M., et al. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-3656 · Cited by 35 · see citing works
Hermand, P., Azouzi, S., Gautier, E., Guillonneau, F., Bondet, V., Duffy, D., Dechavanne, S., Tharaux, P., Mayeux, P., Kim, C. L. V., et al. (2020) · Haematologica · doi:10.3324/haematol.2019.238295 · Cited by 34 · see citing works
- Authors
- Bancerek, J., Poss, Z. C., Steinparzer, I., Sedlyarov, V., Pfaffenwimmer, T., Mikulic, I., Dölken, L., Strobl, B., Müller, M., Taatjes, D. J., & Kovarik, P.
- Affiliations
- University of Vienna (AT)
- University of Colorado Boulder (US)
- University of Cambridge (GB)
- University of Veterinary Medicine Vienna (AT)
- Corresponding author
- Kovarik, Pavel
- ORCID
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2013-02
- Volume
- 38
- Issue
- 2
- Pages
- 250-262
- ISSN
- 1074-7613 (ISSN-L)
- PMC
- PMC3580287
- OpenAlex
- W2059553622
- Cited by
- 297
- References
- 53
- Citations by year
- 2026: 32 · 2025: 28 · 2024: 29 · 2023: 21 · 2022: 23 · 2021: 20 · 2020: 24 · 2019: 27 · 2018: 19 · 2017: 24 · 2016: 15 · 2015: 13 · 2014: 13 · 2013: 9
- FWCI
- 8.93
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Immunity (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Funders
- Austrian Science Fund
- Universität Wien
- National Institutes of Health
- National Cancer Institute (R01CA127364, P30CA046934)
- National Institute of General Medical Sciences (T32-GM08759, T32GM008759, T32GM142607)
- Topics
- Health Sciences › Medicine › Oncology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Keywords
- CDK8, STAT1, STAT3, STAT5, serine phosphorylation, transactivation domain, Mediator complex, interferon signaling, interferon-gamma, antiviral response, RNA polymerase II occupancy, gene expression regulation
- MeSH terms
- Animals, Fibroblasts, Gene Expression Regulation, Humans, Interferon-gamma, Phosphorylation, Promoter Regions, Genetic, RNA Polymerase II, Transcription, Genetic, Signal Transduction, Interleukin-6, Vesiculovirus, Oligonucleotide Array Sequence Analysis, STAT1 Transcription Factor, STAT3 Transcription Factor, STAT5 Transcription Factor, Mice, Cyclin-Dependent Kinase 8, Hep G2 Cells
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